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Volumn 179, Issue 4, 1997, Pages 1337-1343

MalFGK complex assembly and transport and regulatory characteristics of MalK insertion mutants

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CYTOPLASM PROTEIN; MALTOSE;

EID: 0031039347     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.4.1337-1343.1997     Document Type: Article
Times cited : (32)

References (23)
  • 1
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amann, E., B. Ochs, and K. J. Abel. 1988. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69:301-315.
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.J.3
  • 2
    • 0001769249 scopus 로고    scopus 로고
    • Periplasmic binding protein-dependent ABC transporters
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, R. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.). ASM Press, Washington, D.C.
    • Boos, W., and J. M. Lucht. 1996. Periplasmic binding protein-dependent ABC transporters, p. 1175-1209. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, R. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 1175-1209
    • Boos, W.1    Lucht, J.M.2
  • 3
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in E. coli using bacteriophage lambda and mu
    • Casadaban, M. 1976. Transposition and fusion of the lac genes to selected promoters in E. coli using bacteriophage lambda and mu. J. Mol. Biol. 104:541-555.
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.1
  • 4
    • 0025738363 scopus 로고
    • Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli
    • Davidson, A. L., and H. Nikaido. 1991. Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli. J. Biol. Chem. 266:8946-8951.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8946-8951
    • Davidson, A.L.1    Nikaido, H.2
  • 5
    • 0025687504 scopus 로고
    • Regulation of the maltose transport system of Escherichia coli by the glucose-specific enzyme III of the phosphoenolpyruvate-sugar phosphotransferase system
    • Dean, D. A., J. Reizer, H. Nikaido, and M. H. Saier, Jr. 1990. Regulation of the maltose transport system of Escherichia coli by the glucose-specific enzyme III of the phosphoenolpyruvate-sugar phosphotransferase system. J. Biol. Chem. 265:21005-21010.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21005-21010
    • Dean, D.A.1    Reizer, J.2    Nikaido, H.3    Saier Jr., M.H.4
  • 6
    • 0024380890 scopus 로고
    • Maltose transport in membrane vesicles of E. coli is linked to ATP hydrolysis
    • Dean, D. A., A. L. Davidson, and H. Nikaido. 1989. Maltose transport in membrane vesicles of E. coli is linked to ATP hydrolysis. Proc. Natl. Acad. Sci. USA 86:9134-9138.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9134-9138
    • Dean, D.A.1    Davidson, A.L.2    Nikaido, H.3
  • 7
    • 0019332779 scopus 로고
    • Mutations affecting localization of an Escherichia coli outer membrane protein, the bacteriophage λ receptor
    • Emr, S. D., and T. J. Silhavy. 1980. Mutations affecting localization of an Escherichia coli outer membrane protein, the bacteriophage λ receptor. J. Mol. Biol. 141:63-90.
    • (1980) J. Mol. Biol. , vol.141 , pp. 63-90
    • Emr, S.D.1    Silhavy, T.J.2
  • 9
    • 0025904264 scopus 로고
    • The activities of the Escherichia coli MalK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations
    • Kühnau, S., M. Reyes, A. Sievertsen, H. A. Shuman, and W. Boos. 1991. The activities of the Escherichia coli MalK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations. J. Bacteriol. 173:2180-2186.
    • (1991) J. Bacteriol. , vol.173 , pp. 2180-2186
    • Kühnau, S.1    Reyes, M.2    Sievertsen, A.3    Shuman, H.A.4    Boos, W.5
  • 10
    • 0028134990 scopus 로고
    • Mutations eliminating the protein export function of a membrane-spanning sequence
    • Lee, E., and C. Manoil. 1994. Mutations eliminating the protein export function of a membrane-spanning sequence. J. Biol. Chem. 269:28822-28828.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28822-28828
    • Lee, E.1    Manoil, C.2
  • 11
    • 0025020688 scopus 로고
    • Analysis of protein localization by use of gene fusions with complementary properties
    • Manoil, C. 1990. Analysis of protein localization by use of gene fusions with complementary properties. J. Bacteriol. 172:1035-1042.
    • (1990) J. Bacteriol. , vol.172 , pp. 1035-1042
    • Manoil, C.1
  • 12
    • 85035186259 scopus 로고    scopus 로고
    • A simple screen for permissive sites in proteins: Analysis of Escherichia coli lac permease
    • in press
    • Manoil, C., and J. Bailey. A simple screen for permissive sites in proteins: analysis of Escherichia coli lac permease. J. Mol. Biol., in press.
    • J. Mol. Biol.
    • Manoil, C.1    Bailey, J.2
  • 13
  • 14
    • 85035185547 scopus 로고
    • Structural model of the nucleotide-binding conserved component of periplasmic permeases
    • Mimura, C. S., S. R. Holbrook, and G. F.-L. Ames. 1991. Structural model of the nucleotide-binding conserved component of periplasmic permeases. Proc. Natl. Acad. Sci. USA 84:2688-2692.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2688-2692
    • Mimura, C.S.1    Holbrook, S.R.2    Ames, G.F.-L.3
  • 16
    • 0027375813 scopus 로고
    • Characterization of the structural requirements for assembly and nucleotide binding of an ATP-binding cassette transporter
    • Panagiotidis, C. H., M. Reyes, A. Sievertsen, W. Boos, and H. A. Shuman. 1993. Characterization of the structural requirements for assembly and nucleotide binding of an ATP-binding cassette transporter. J. Biol. Chem. 268:23685-23696.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23685-23696
    • Panagiotidis, C.H.1    Reyes, M.2    Sievertsen, A.3    Boos, W.4    Shuman, H.A.5
  • 17
    • 0024095619 scopus 로고
    • Overproduction of MatK protein prevents expression of the E. coli mal regulon
    • Reyes, M., and H. A. Shuman. 1988. Overproduction of MatK protein prevents expression of the E. coli mal regulon, J. Bacteriol. 170:4598-4602.
    • (1988) J. Bacteriol. , vol.170 , pp. 4598-4602
    • Reyes, M.1    Shuman, H.A.2
  • 18
    • 0017802555 scopus 로고
    • Permease-specific mutations in Salmonella typhimurium and Escherichia coli that release the glycerol, maltose, melibiose, and lactose transport systems from regulation by the phosphoenolpyruvate:sugar phosphotransferase system
    • Saier, M. H., H. Straud, L. S. Massman, J. D. Judice, M. H. Newman, and B. U. Feucht. 1978. Permease-specific mutations in Salmonella typhimurium and Escherichia coli that release the glycerol, maltose, melibiose, and lactose transport systems from regulation by the phosphoenolpyruvate:sugar phosphotransferase system. J. Bacteriol. 133:1358-1367.
    • (1978) J. Bacteriol. , vol.133 , pp. 1358-1367
    • Saier, M.H.1    Straud, H.2    Massman, L.S.3    Judice, J.D.4    Newman, M.H.5    Feucht, B.U.6
  • 20
    • 0025740666 scopus 로고
    • A chimeric nucleotide-binding protein, encoded by a hisP-malK hybrid gene, is functional in maltose transport in Salmonella typhimurium
    • Schneider, E., and C. Walter. 1991. A chimeric nucleotide-binding protein, encoded by a hisP-malK hybrid gene, is functional in maltose transport in Salmonella typhimurium. Mol. Microbiol. 5:1375-1383.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1375-1383
    • Schneider, E.1    Walter, C.2
  • 21
    • 0028109264 scopus 로고
    • Nucleotide-induced conformational changes of MalK, a bacterial ATP binding cassette transporter protein
    • Schneider, E., S. Wilken, and R. Schmid. 1994. Nucleotide-induced conformational changes of MalK, a bacterial ATP binding cassette transporter protein. J. Biol. Chem. 269:20456-20461.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20456-20461
    • Schneider, E.1    Wilken, S.2    Schmid, R.3
  • 22
    • 0026469992 scopus 로고
    • The assembly of a hetero-oligomeric membrane protein complex
    • Traxler, B., and J. Beckwith. 1992. The assembly of a hetero-oligomeric membrane protein complex. Proc. Natl. Acad. Sci. USA 89:10852-10856.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10852-10856
    • Traxler, B.1    Beckwith, J.2
  • 23
    • 0027126818 scopus 로고
    • Characterization of site-directed mutations in conserved domains of MalK, a bacterial member of the ATP-binding cassette (ABC) family
    • Walter, C., S. Wilken, and E. Schneider. 1992. Characterization of site-directed mutations in conserved domains of MalK, a bacterial member of the ATP-binding cassette (ABC) family. FEBS Lett. 303:41-44.
    • (1992) FEBS Lett. , vol.303 , pp. 41-44
    • Walter, C.1    Wilken, S.2    Schneider, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.